Co-chaperones are proteins that assist chaperones in protein folding and other functions. Co-chaperones are the non-client binding molecules that assist in protein folding mediated by Hsp70 and Hsp90. They are particularly essential in stimulation of the ATPase activity of these chaperone proteins. There are a great number of different co-chaperones however based on their domain structure most of them fall into two groups: J-domain proteins and tetratricopeptide repeats (TPR).[1]
Co-chaperones assist heat shock proteins in the protein folding process. These co-chaperones can function in a number of ways. Primarily co-chaperones are involved in the ATPase functionality of their associated heat shock proteins. Co-chaperones catalyze the hydrolysis ATP to ADP on their respective chaperones which then allows them undergo a large conformational change that allows them to either bind to their substrates with higher affinity or aid in the release of the substrate following protein folding, as in the case of co-chaperone p23.[2]
J-proteins, DnaJ or Hsp40 are important co-chaperones for Hsp70 and have the ability to bind to polypeptides and then recruit chaperone protein DnaK and passes the polypeptide along to this chaperone by catalyzing ATP hydrolysis that allows DnaK to bind to the unfolded polypeptide with high affinity. Another co-chaperone, GrpE, comes in following the folding of this protein to cause a conformational change in DnaK that allows it to release the folded protein.[3] The mechanism of TPR proteins is less studied these domains have been shown to interact with Hsp90 and Hsp70 and may be involved in the creation of an Hsp70-Hsp90 multi-chaperone complex.[4]
Co-chaperones may also play an important role in misfolding diseases such as cystic fibrosis. An interaction between Hsp90 and its co-chaperone, Aha1, is essential to the proper folding of cystic fibrosis transmembrane conductance regulator (CFTR).[5] Other examples of co-chaperone's role in illness include neurodegenerative diseases. Alzheimer’s and Parkinson’s disease have a number of proteins that can aggregate if not properly chaperoned. Co-chaperones CSPα (DNAJC5), auxilin (DNAJC6) and RME-8 (DNAJC13) are important for preserving folding and assembly, therefore preventing protein aggregation.[6] Detection of mutations in these proteins have been associated with the early onset of neurodegenerative diseases.[7]
^Caplan AJ (2017-05-28). "What is a co-chaperone?". Cell Stress & Chaperones. 8 (2): 105–7. PMC514860. PMID 14627194.
^Young JC, Hartl FU (November 2000). "Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23". The EMBO Journal. 19 (21): 5930–40. doi:10.1093/emboj/19.21.5930. PMC305790. PMID 11060043.
^Langer T, Lu C, Echols H, Flanagan J, Hayer MK, Hartl FU (April 1992). "Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding". Nature. 356 (6371): 683–9. Bibcode:1992Natur.356..683L. doi:10.1038/356683a0. PMID 1349157. S2CID 4324738.
^Scheufler C, Brinker A, Bourenkov G, Pegoraro S, Moroder L, Bartunik H, Hartl FU, Moarefi I (2000). "Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine". Cell. 101 (2): 199–210. doi:10.1016/S0092-8674(00)80830-2. PMID 10786835.
^Olgiati S, Quadri M, Fang M, Rood JP, Saute JA, Chien HF, et al. (February 2016). "DNAJC6 Mutations Associated With Early-Onset Parkinson's Disease". Annals of Neurology. 79 (2): 244–56. doi:10.1002/ana.24553. PMID 26528954. S2CID 20940327.
^Gorenberg EL, Chandra SS (2017). "The Role of Co-chaperones in Synaptic Proteostasis and Neurodegenerative Disease". Frontiers in Neuroscience. 11: 248. doi:10.3389/fnins.2017.00248. PMC5437171. PMID 28579939.
Further readingEdit
Young JC, Barral JM, Ulrich Hartl F (October 2003). "More than folding: localized functions of cytosolic chaperones". Trends in Biochemical Sciences. 28 (10): 541–7. doi:10.1016/j.tibs.2003.08.009. PMID 14559183.
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Co chaperones are proteins that assist chaperones in protein folding and other functions Co chaperones are the non client binding molecules that assist in protein folding mediated by Hsp70 and Hsp90 They are particularly essential in stimulation of the ATPase activity of these chaperone proteins There are a great number of different co chaperones however based on their domain structure most of them fall into two groups J domain proteins and tetratricopeptide repeats TPR 1 Co chaperones assist heat shock proteins in the protein folding process These co chaperones can function in a number of ways Primarily co chaperones are involved in the ATPase functionality of their associated heat shock proteins Co chaperones catalyze the hydrolysis ATP to ADP on their respective chaperones which then allows them undergo a large conformational change that allows them to either bind to their substrates with higher affinity or aid in the release of the substrate following protein folding as in the case of co chaperone p23 2 J proteins DnaJ or Hsp40 are important co chaperones for Hsp70 and have the ability to bind to polypeptides and then recruit chaperone protein DnaK and passes the polypeptide along to this chaperone by catalyzing ATP hydrolysis that allows DnaK to bind to the unfolded polypeptide with high affinity Another co chaperone GrpE comes in following the folding of this protein to cause a conformational change in DnaK that allows it to release the folded protein 3 The mechanism of TPR proteins is less studied these domains have been shown to interact with Hsp90 and Hsp70 and may be involved in the creation of an Hsp70 Hsp90 multi chaperone complex 4 Co chaperones may also play an important role in misfolding diseases such as cystic fibrosis An interaction between Hsp90 and its co chaperone Aha1 is essential to the proper folding of cystic fibrosis transmembrane conductance regulator CFTR 5 Other examples of co chaperone s role in illness include neurodegenerative diseases Alzheimer s and Parkinson s disease have a number of proteins that can aggregate if not properly chaperoned Co chaperones CSPa DNAJC5 auxilin DNAJC6 and RME 8 DNAJC13 are important for preserving folding and assembly therefore preventing protein aggregation 6 Detection of mutations in these proteins have been associated with the early onset of neurodegenerative diseases 7 Contents 1 List of co chaperones 2 See also 3 References 4 Further readingList of co chaperones EditAha1 auxilin BAG1 CAIR 1 Bag 3 CDC37 p50 Chp1 Cysteine string protein CSP Cyp40 Djp1 DnaJ E3 E4 ubiquitin ligase FKBP4 GAK GroES GrpE Hch1 Hip Hsc70 interacting protein ST13 Hop Hsp70 Hsp90 organizing protein STIP1 Mrj PP5 Sacsin SGT Snl1 SODD Bag 4 Swa2 Aux1 Tom34 Tom70 UNC 45 WISp39See also EditChaperone protein Heat shock proteinReferences Edit Caplan AJ 2017 05 28 What is a co chaperone Cell Stress amp Chaperones 8 2 105 7 PMC 514860 PMID 14627194 Young JC Hartl FU November 2000 Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co chaperone p23 The EMBO Journal 19 21 5930 40 doi 10 1093 emboj 19 21 5930 PMC 305790 PMID 11060043 Langer T Lu C Echols H Flanagan J Hayer MK Hartl FU April 1992 Successive action of DnaK DnaJ and GroEL along the pathway of chaperone mediated protein folding Nature 356 6371 683 9 Bibcode 1992Natur 356 683L doi 10 1038 356683a0 PMID 1349157 S2CID 4324738 Scheufler C Brinker A Bourenkov G Pegoraro S Moroder L Bartunik H Hartl FU Moarefi I 2000 Structure of TPR domain peptide complexes critical elements in the assembly of the Hsp70 Hsp90 multichaperone machine Cell 101 2 199 210 doi 10 1016 S0092 8674 00 80830 2 PMID 10786835 Wang X Venable J LaPointe P Hutt DM Koulov AV Coppinger J Gurkan C Kellner W Matteson J Plutner H Riordan JR Kelly JW Yates JR Balch WE November 2006 Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis Cell 127 4 803 15 doi 10 1016 j cell 2006 09 043 PMID 17110338 Olgiati S Quadri M Fang M Rood JP Saute JA Chien HF et al February 2016 DNAJC6 Mutations Associated With Early Onset Parkinson s Disease Annals of Neurology 79 2 244 56 doi 10 1002 ana 24553 PMID 26528954 S2CID 20940327 Gorenberg EL Chandra SS 2017 The Role of Co chaperones in Synaptic Proteostasis and Neurodegenerative Disease Frontiers in Neuroscience 11 248 doi 10 3389 fnins 2017 00248 PMC 5437171 PMID 28579939 Further reading EditYoung JC Barral JM Ulrich Hartl F October 2003 More than folding localized functions of cytosolic chaperones Trends in Biochemical Sciences 28 10 541 7 doi 10 1016 j tibs 2003 08 009 PMID 14559183 This protein related article is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title Co chaperone amp oldid 1116603995, wikipedia, wiki, book, books, library,
